Tracking interactions that stabilize the dimer structure of starch phosphorylase from Corynebacterium callunae. Roles of Arg234 and Arg242 revealed by sequence analysis and site-directed mutagenesis. [electronic resource]
Producer: 20030627Description: 2126-36 p. digitalISSN:- 0014-2956
- Allosteric Site
- Amino Acid Sequence
- Arginine -- chemistry
- Binding Sites
- Blotting, Southern
- Circular Dichroism
- Cloning, Molecular
- Corynebacterium -- enzymology
- DNA -- metabolism
- Dimerization
- Escherichia coli -- metabolism
- Gene Library
- Glucans -- metabolism
- Hydrogen-Ion Concentration
- Kinetics
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Oligonucleotides -- pharmacology
- Plasmids -- metabolism
- Protein Structure, Quaternary
- Protein Structure, Tertiary
- Recombinant Proteins -- chemistry
- Sequence Homology, Amino Acid
- Starch Phosphorylase -- chemistry
- Temperature
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Publication Type: Journal Article; Research Support, Non-U.S. Gov't
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